Analytical Data
-
Gene name
QKI
- Application
-
Alternative Names
HKQ
-
Species
Human
-
Source
E. coli
-
Tag
Strep;His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96PU8-1
-
Expression Region
T7-L214
-
Protein Length
Partial
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
QKI (Quaking-Induced Protein) is an essential RNA-binding protein that plays a critical role in the regulation of gene expression and RNA processing, particularly in the context of neural development and myelination. Its expression is prominently observed in oligodendrocytes, where it is vital for the development of myelin sheaths around neurons, thereby influencing neuronal signaling and function. The QKI gene undergoes alternative splicing, leading to the production of multiple isoforms with distinct functional properties. Recent studies have suggested that dysregulation of QKI may be implicated in various neurological disorders, including schizophrenia, multiple sclerosis, and other demyelinating diseases. The investigation of QKI recombinant proteins has gained significant interest as it provides insights into the mechanisms underlying its diverse biological functions. Researchers utilize recombinant QKI proteins to study RNA-protein interactions, elucidate the molecular pathways involved in myelination, and assess the impact of specific QKI isoforms on cellular processes. This research not only enhances our understanding of fundamental biological mechanisms but also holds potential for developing therapeutic strategies aimed at addressing neurological disorders associated with QKI dysfunction. The exploration of QKI’s role in cellular and molecular contexts continues to provide vital knowledge that could pave the way for innovative treatments and interventions in neurodegenerative conditions.
